ID A0A2A2L933_9BILA Unreviewed; 1212 AA.
AC A0A2A2L933;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Deoxyhypusine hydroxylase {ECO:0000256|HAMAP-Rule:MF_03101};
DE Short=DOHH {ECO:0000256|HAMAP-Rule:MF_03101};
DE EC=1.14.99.29 {ECO:0000256|HAMAP-Rule:MF_03101};
DE AltName: Full=Deoxyhypusine dioxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
DE AltName: Full=Deoxyhypusine monooxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
GN ORFNames=WR25_24723 {ECO:0000313|EMBL:PAV82781.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV82781.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV82781.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV82781.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC lysine intermediate to form hypusine, an essential post-translational
CC modification only found in mature eIF-5A factor. {ECO:0000256|HAMAP-
CC Rule:MF_03101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-
CC hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144,
CC Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657,
CC ChEBI:CHEBI:91175; EC=1.14.99.29;
CC Evidence={ECO:0000256|ARBA:ARBA00000068, ECO:0000256|HAMAP-
CC Rule:MF_03101};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03101};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03101};
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC {ECO:0000256|ARBA:ARBA00005041, ECO:0000256|HAMAP-Rule:MF_03101}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000256|HAMAP-Rule:MF_03101}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV82781.1}.
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DR EMBL; LIAE01007028; PAV82781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2L933; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005761; C:mitochondrial ribosome; IEA:InterPro.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR CDD; cd02557; PseudoU_synth_ScRIB2; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR019368; Ribosomal_mS29.
DR InterPro; IPR008092; Ribosomal_mS29_met.
DR NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR Pfam; PF10236; DAP3; 1.
DR Pfam; PF13646; HEAT_2; 2.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR PRINTS; PR01716; DEATHASSOCP3.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 3: Inferred from homology;
KW Hypusine biosynthesis {ECO:0000256|ARBA:ARBA00023256, ECO:0000256|HAMAP-
KW Rule:MF_03101};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03101};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03101};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_03101};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03101}; Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1085..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1162..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..195
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
FT REPEAT 452..492
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
FT BINDING 438
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 439
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 471
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 472
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 589
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 590
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 622
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT BINDING 623
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
SQ SEQUENCE 1212 AA; 139003 MW; F9FFBEF99B0566FC CRC64;
MGRMFVNGEQ MTDINYVFKH NDRVEHWMHR HEHPVLDLPI RIINEDENLL VVDKPPSMPV
HACGQYNTNT IMGQLRQNKM ADKDLRVLHR LDRTTSGILL FAKNYATDLE FKTTLKDGHW
RKTYVCKVEG EFPEGAVFCD QPIGNLVISM GIQCVRPDGK PARSKFRRMW TNGKESVVEV
TIDTGRTHQI RVHAQFLGYP LIDDKIYNSR NWGEQKGKNA EYGKSYEELA EIIRVNHRSE
NWMEYKNPEY DQMMEDIAAK LDEITPDDPN IRPEDRPSTD KICLNCNVRK KVPQMADFRM
PLHCLRYETD KWSFQTELPD WARESGGQVP ESVPNQPILE TDHADQVPES SLQNSELEKF
QNSSNQNVQL KIGFKFQKIM EAKFSKDDIG KFGRVLCDTR YPLKARFRAL FILRNIGDDL
SVDWISNAFD DESALLKHEL AYCLGQMKNK SAIPILETIL RDKNQEPMVR HEAGEALGAI
GDPSSREILK EYKNDPQPEV AETCDLALKR IDWIIESGKD TDSPYQSVDP TPTSSSDSIE
ILGKTLIDLK RPLWERYQAM FKLRNINTDE SIKALAQGLY CEDSALFRHE IAYVLGQVQS
PVATKELKDR LLLEEENCMV RHECAEALGA IATDECTEIL KTYAKDKERV VRESCEVALD
MAEYENSDEL QQAAFVAKRR FQTSSRALKE NYPKLTSFTD SDIGKMYEID IETARQLQYD
KQLTLKLKAQ VETLNEMVTV VRKPLVEIAD CMQSVCSVDI PALRLVLWGH FGTGKSVTLS
QAVHLAYSHN WCIVYHPTAM HLCRRLQEVE MSTHKPGRIN DPNGAVAILQ AFKHQNQHLW
KVLSELPCER TYEWSKVDKT QQGKPITEIV EVGLSAPFLA SDCVGALFRE LKRHASSGKI
KLFVGIDDAN SCWGKVNVRR ADRTYALPSD LTLVCHYRNI MKNDWSNGII VAVTDRKEQA
DNRNELEVLP YTPLETLGEE GFDHLDPFLP IECVEYSETE VTAVYNYYKD RRWISHSKAL
TDSGKLEMMH LSGFNPFYFE RLCAGGSKML PIMGDTTPPA PPARNVSTFP AKVTFKGAQT
WRESLGMFMI LLLGMSAFIS VIILCVYTWK DKQVYEELVN YMDTTISISK IQYNPQYGIY
NLNDRELDVL GRERSYKNLL RGYLFAEFGF WGLLIAVAFV YMTTDLTVQA KKIVFWVNIS
NSIIQLTHYF II
//
